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The enzymes involved in the synthesis of phytic acid inLemna gibba(Studies on the biosynthesis of cyclitols, XL.)

✍ Scribed by Otto Bollmann; Stanley Strother; Otto Hoffmann-Ostenhof


Publisher
Springer
Year
1980
Tongue
English
Weight
374 KB
Volume
30
Category
Article
ISSN
0300-8177

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✦ Synopsis


The biosynthesis of phytic acid is known to be catalyzed by enzymes causing a stepwise phosphorylation of myo-inositol or 1L-myo-inositol 1-phosphate with adenosine triphosphate as phosphate donor. The kinase responsible for these phosphorylations in Lemna gibba were purified by affinity chromatography on a Sepharose gel carrying myo-inositol 2-phosphate at the binding site. Three fractions with enzymatic activity could be identified; in the first one, we find myo-inositol kinase (EC 2.7.1.64) phosphorylating myo-inositol to 1L-myo-inositol 1-phosphate; the second one brings about the phosphorylation of myo-inositol trisphosphate to phytic acid; the third one phosphorylates myo-inositol 1-phosphate to a myo-inositol trisphosphate. An enzyme oxidizing 1L-myo-inositol 1-phosphate to an uronic acid derivative is found in the first two fractions. In the presence of ATP, Mg2+, Mn2+, and the second and the third enzyme fractions in an appropraite mixture, 1L-myo-inositol 1-phosphate can be phosphorylated to phytic acid. The structure of the trisphosphate acting as an intermediate is not yet known.


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